arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 - Protein

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A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor. [Curr Biol. 2006]
A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor.
Nie Z, Hirsch DS, Luo R, Jian X, Stauffer S, Cremesti A, Andrade J, Lebowitz J, Marino M, Ahvazi B, et al. Curr Biol. 2006 Jan 24; 16(2):130-9.
Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site. [J Biol Chem. 2000]
Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site.
Kam JL, Miura K, Jackson TR, Gruschus J, Roller P, Stauffer S, Clark J, Aneja R, Randazzo PA. J Biol Chem. 2000 Mar 31; 275(13):9653-63.
ASAP1 promotes tumor cell motility and invasiveness, stimulates metastasis formation in vivo, and correlates with poor survival in colorectal cancer patients. [Oncogene. 2010]
ASAP1 promotes tumor cell motility and invasiveness, stimulates metastasis formation in vivo, and correlates with poor survival in colorectal cancer patients.
Müller T, Stein U, Poletti A, Garzia L, Rothley M, Plaumann D, Thiele W, Bauer M, Galasso A, Schlag P, et al. Oncogene. 2010 Apr 22; 29(16):2393-403. Epub 2010 Feb 15.

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